Yamamoto Yasuhiko, Terui Norifumi, Tachiiri Naoki, Minakawa Kazuhisa, Matsuo Hitomi, Kameda Tsunenori, Hasegawa Jun, Sambongi Yoshihiro, Uchiyama Susumu, Kobayashi Yuji, Igarashi Yasuo
Department of Chemistry, University of Tsukuba, Tsukuba 305-8571, Japan.
J Am Chem Soc. 2002 Oct 2;124(39):11574-5. doi: 10.1021/ja025597s.
Paramagnetic NMR and optical studies of the oxidized forms of mesophile Pseudomonas aeruginosa cytochrome c(551) and its quintuple mutant (F7A/V13M/F34Y/E43Y/V78I), and thermophile Hydrogenobacter thermophilus cytochrome c(552) demonstrated that the amino acid side chain packings in the protein interior influence the coordination bond between the heme iron and the axial methionine in the proteins. The strength of heme axial coordinations was found to correlate with the overall protein thermostability.
嗜温性铜绿假单胞菌细胞色素c(551)及其五重突变体(F7A/V13M/F34Y/E43Y/V78I)氧化形式的顺磁核磁共振和光学研究，以及嗜热性嗜氢菌细胞色素c(552)的研究表明，蛋白质内部的氨基酸侧链堆积影响蛋白质中血红素铁与轴向甲硫氨酸之间的配位键。发现血红素轴向配位的强度与蛋白质的整体热稳定性相关。
